About: Molecular dynamics simulations of glycosyltransferase LgtC

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Molecular dynamics simulations have been performed on fully solvated alpha-(1->4)-galactosyltransferase LgtC from Neisseria meningitidis with and without the donor substrate UDP-Gal and in the presence of the manganese ion. The analysis of the trajectories revealed a limited movement in the loop X (residues 75-80) and a larger conformational change in the loop Y (residues 246-251) in the simulation, when UDP-Gal was not present. In this case, the loops X and Y open by almost 10 A, exposing the active site to the solvent. The 'hinge region' responsible for the opening is composed of residues 246-247. We have also analyzed the behavior of the manganese ion in the simulations. The coordination number is 6 when UDP-Gal is present and it increases to 7 when it is absent. In the latter case, three water molecules become coordinated to the ion. In both cases, the coordination is very stable implying that the manganese ion is tightly bound in the active site of the enzyme even if UDP-Gal is not present. Fu Molecular dynamics simulations have been performed on fully solvated alpha-(1->4)-galactosyltransferase LgtC from Neisseria meningitidis with and without the donor substrate UDP-Gal and in the presence of the manganese ion. The analysis of the trajectories revealed a limited movement in the loop X (residues 75-80) and a larger conformational change in the loop Y (residues 246-251) in the simulation, when UDP-Gal was not present. In this case, the loops X and Y open by almost 10 A, exposing the active site to the solvent. The 'hinge region' responsible for the opening is composed of residues 246-247. We have also analyzed the behavior of the manganese ion in the simulations. The coordination number is 6 when UDP-Gal is present and it increases to 7 when it is absent. In the latter case, three water molecules become coordinated to the ion. In both cases, the coordination is very stable implying that the manganese ion is tightly bound in the active site of the enzyme even if UDP-Gal is not present. Fu (en) MD simulace glycosyltransferasy LgtC (cs)
Title	MD simulace glycosyltransferasy LgtC (cs) Molecular dynamics simulations of glycosyltransferase LgtC Molecular dynamics simulations of glycosyltransferase LgtC (en)
skos:prefLabel	MD simulace glycosyltransferasy LgtC (cs) Molecular dynamics simulations of glycosyltransferase LgtC Molecular dynamics simulations of glycosyltransferase LgtC (en)
skos:notation	RIV/00216224:14310/04:00009950!RIV08-MSM-14310___
http://linked.open.../vavai/riv/strany	995-1006
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(LN00A016)
http://linked.open...iv/cisloPeriodika	5
http://linked.open...vai/riv/dodaniDat	2008
http://linked.open...aciTvurceVysledku	Kulhánek, Petr Koča, Jaroslav Šnajdrová, Lenka
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	574370
http://linked.open...ai/riv/idVysledku	RIV/00216224:14310/04:00009950
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Galactosyltransferase; Molecular dynamics; Loops opening; Structural water molecules (en)
http://linked.open.../riv/klicoveSlovo	Molecular dynamics Loops opening Structural water molecules Galactosyltransferase
http://linked.open...odStatuVydavatele	NL - Nizozemsko
http://linked.open...ontrolniKodProRIV	[E75403F08BC1]
http://linked.open...i/riv/nazevZdroje	Carbohydrate Research
http://linked.open...in/vavai/riv/obor	CC
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...vavai/riv/projekt	BIOMOLECULAR CENTER
http://linked.open...UplatneniVysledku	2004
http://linked.open...v/svazekPeriodika	339
http://linked.open...iv/tvurceVysledku	Imberty, Anne Koča, Jaroslav Kulhánek, Petr Šnajdrová, Lenka
issn	0008-6215
number of pages	12 (xsd:int)
http://localhost/t...ganizacniJednotka	14310

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